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1-naphthyl phosphate + H2O
1-naphthol + phosphate
2-glycerophosphate + H2O
glycerate + phosphate
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
3-phosphoglycerate + H2O
glycerate + phosphate
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
5'-ATP + H2O
?
-
250% of the activity with myo-inositol hexakisphosphate
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
alpha-glycerophosphate + H2O
glycerol + phosphate
AMP + H2O
adenosine + phosphate
AMP + phosphate
adenosine + phosphate
-
43.9% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
bis(p-nitrophenyl)phosphate + H2O
?
-
-
-
-
?
D-fructose 1,6-diphosphate + H2O
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
D-glucose 1-phosphate + H2O
D-glucose + phosphate
D-glucose 6-phosphate + H2O
D-glucose + phosphate
D-glucose 6-phosphate + H2O
glucose + phosphate
-
reaction is nearly as efficient as on phytate
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
50% of the activity with myo-inositol hexakisphosphate
-
?
diphosphate + H2O
2 phosphate
fructose 1,6-bisphosphate + H2O
?
-
-
-
?
fructose 1,6-diphosphate + H2O
?
glucose 1-phosphate + H2O
glucose + phosphate
Glucose 6-phosphate + H2O
Glucose + phosphate
glycerol 2-phosphate + H2O
glycerol + phosphate
glycerol 3-phosphate + H2O
glycerol + phosphate
inositol 1,4-diphosphate + H2O
?
-
-
-
-
?
inositol pentakisphosphate + H2O
?
inositol tetrakisphosphate + H2O
?
-
-
-
-
?
inositol-1-phosphate + H2O
inositol + phosphate
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
? + phosphate
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,3,4,5-pentaphosphate + phosphate
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,4,5,6-pentaphosphate + phosphate
myo-inositol hexakisphosphate + H2O
L-myo-inositol 1,2,3,4,5-pentakisphosphate + myo-inositol 1,2,3,4,6-pentakisphosphate + myo-inositol 1,3,4,5,6-pentakisphosphate + myo-inositol 2-phosphate + D-myo-inositol 1,2-bisphosphate + L-myo-inositol 1,2-bis phosphate + L-myo-inositol 1,2,3,4-tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
myo-inositol trikisphosphate + H2O
?
myo-inositol-1,2,3,4,5 pentakisphosphate + H2O
?
-
12% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
myo-inositol-1,2,3,4,6 pentakisphosphate + H2O
?
-
22% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
-
-
?
myo-inositol-1,2,4,5,6 pentakisphosphate + H2O
?
-
16% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
-
-
?
myo-inositol-1,3,4,5,6 pentakisphosphate + H2O
?
-
27% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
-
-
?
myo-inositol-5-phosphate + H2O
inositol + phosphate
-
18% of the activity with myo-inositol hexakisphosphate
-
-
?
NADP+ + H2O
NAD+ + phosphate
O-phospho-L-Ser + H2O
Ser + phosphate
O-phospho-L-serine + H2O
L-serine + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
phenyl phosphate
phenol + phosphate
phenyl phosphate + H2O
phenol + phosphate
phosphoenol pyruvate + H2O
?
-
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
polyphosphate + H2O
?
-
-
-
-
?
pyridoxal phosphate + H2O
pyridoxal + phosphate
tetrasodium diphosphate + H2O
?
additional information
?
-
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
74% of the activity with myo-inositol hexakisphosphate
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
130% of the activity with myo-inositol hexakisphosphate
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
89.6% of the activity with myo-inositol hexakisphosphate
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
63.6% of the activity with myo-inositol hexakisphosphate
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
97.1% of the activity with myo-inositol hexakisphosphate
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
-
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
39.8% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
11% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
11% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
101% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
59.6% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
reaction is nearly as efficient as on phytate
-
?
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
ADP + H2O
?
-
25.6% of the activity with myo-inositol hexakisphosphate
-
?
ADP + H2O
?
-
14.2% of the activity with myo-inositol hexakisphosphate
-
?
alpha-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
alpha-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
?
AMP + H2O
adenosine + phosphate
-
9.7fold higher activity than with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
25.0% of the activity with myo-inositol hexakisphosphate
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
ATP + H2O
?
-
-
-
?
ATP + H2O
?
-
38.8% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
?
-
22.3% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
?
-
reaction is nearly as efficient as on phytate
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
146% of the activity with myo-inositol hexakisphosphate
-
?
D-fructose 1,6-diphosphate + H2O
?
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
28.6% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
92.0% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
78.5% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
438.5% of the activity with myo-inositol hexakisphosphate
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
735fold higher activity than with myo-inositol hexakisphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
50.8% of the activity with myo-inositol hexakisphosphate
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
19fold higher activity than with myo-inositol hexakisphosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
85.6% of the activity with myo-inositol hexakisphosphate
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 3-phosphate + H2O
glycerol + phosphate
-
15fold higher activity than with myo-inositol hexakisphosphate
-
-
?
glycerol 3-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
GTP + H2O
?
-
-
-
-
?
inositol pentakisphosphate + H2O
?
-
-
-
-
?
inositol pentakisphosphate + H2O
?
-
-
-
-
?
inositol pentakisphosphate + H2O
?
-
myo-inositol pentakisphosphate
-
-
?
inositol-1-phosphate + H2O
inositol + phosphate
-
-
-
-
?
inositol-1-phosphate + H2O
inositol + phosphate
-
myo-inositol-1-phosphate, 6% of the activity with myo-inositol hexakisphosphate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
strong affinity for sodium phytate as substrate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, preferred substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, preferred substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
absolutely specific for, the phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
absolutely specific for, the phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
substrate is sodium phytate or calcium phytate, phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
substrate is sodium phytate or calcium phytate, phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
product release is the rate limiting step of the reaction
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
product release is the rate limiting step of the reaction
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
product release is the rate limiting step of the reaction
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Aspergillus syndowi
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
rapid equilibrium ordered mechanism in which binding of Ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phythate complex
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
rapid equilibrium ordered mechanism in which binding of Ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phythate complex
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for, no activity on other phosphate esters
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for, no activity on other phosphate esters
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme is able to hydrolyze any of the six phosphate groups of phytate. The reaction is likely to proceed through a direct attack of the metal-bridging water molecule on the phosphorous atom of a substrate and the subsequent stabilization of the pentavalent transition state by the bound calcium ions
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
step-wise hydrolysis of myo-inositol hexakisphosphate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
removal of 5 phosphate residues from each molecule of phytate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
removal of 5 phosphate residues from each molecule of phytate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
hydrolyzes phytate in a stepwise manner
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Penicillium caseoicolum
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for phytate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for phytate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Schwanniomyces castellii
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Schwanniomyces castellii
-
constitutive
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,3,4,5-pentaphosphate + phosphate
-
major degradation product
-
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,3,4,5-pentaphosphate + phosphate
-
major degradation product, plus DL-inositol 1,2,4,5,6-pentaphosphate, DL-inositol 1,2,3,4-tetraphosphate and DL-inositol 1,2,4,6-tetraphosphate
-
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,4,5,6-pentaphosphate + phosphate
-
activity of EC 3.1.3.8, 10-14% of product
-
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,4,5,6-pentaphosphate + phosphate
-
activity of EC 3.1.3.8, 10-14% of product
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
the other isomers of inositol hexaphosphate are hydrolyzed at lower rate in decreasing order: myo-inositol hexakisphosphate, neo-inositol hexakisphosphate, scyllo inositol hexakisphosphate : D-chiro inositol hexakisphosphate, L-chiro inositol hexakisphosphate
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
the phosphate from position 6 is liberated first, followed by the phosphate at positions 5 and 4, or 1 and 3
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate.
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate.
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol trikisphosphate + H2O
?
-
-
-
-
?
myo-inositol trikisphosphate + H2O
?
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
NADP+ + H2O
NAD+ + phosphate
-
-
-
-
?
NADP+ + H2O
NAD+ + phosphate
-
-
-
-
?
O-phospho-L-Ser + H2O
Ser + phosphate
-
-
-
-
?
O-phospho-L-Ser + H2O
Ser + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
little activity for p-nitrophenyl phosphate above pH 4.0
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
little activity for p-nitrophenyl phosphate above pH 4.0
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
6% of the activity with myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
phenyl phosphate
phenol + phosphate
-
-
-
?
phenyl phosphate
phenol + phosphate
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
84% of the activity with myo-inositol hexakisphosphate
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
61.7fold higher activity than with myo-inositol hexakisphosphate
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
89.2% of the activity with myo-inositol hexakisphosphate
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
-
-
-
?
pyridoxal phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal phosphate + H2O
pyridoxal + phosphate
-
-
-
?
pyridoxal phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
pyridoxal phosphate + H2O
pyridoxal + phosphate
-
-
-
-
?
tetrasodium diphosphate + H2O
?
-
6% of the activity with myo-inositol hexakisphosphate
-
?
tetrasodium diphosphate + H2O
?
-
6% of the activity with myo-inositol hexakisphosphate
-
?
additional information
?
-
-
enzyme exhibits phytase and acid phosphatase activity
-
?
additional information
?
-
-
highest activity in cells in the late stationary phase
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl phosphate, beta-glycerophosphate, glucose 6-phosphate, sodium glycerophosphate, AMP, ADP and ATP
-
?
additional information
?
-
-
no activity with 4-nitrophenyl phosphate, beta-glycerophosphate, glucose 6-phosphate, sodium glycerophosphate, AMP, ADP and ATP
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
the enzyme shows broad substrate specificity, but the highest activity is observed with phytic acid. Other substrates are 4-nitrophenyl phosphate, ATP, glucose-6-phosphate, and glycerol-3-phosphate. Phosphate detection by ammonium heptamolybdate reagent
-
-
?
additional information
?
-
the enzyme shows broad substrate specificity, but the highest activity is observed with phytic acid. Other substrates are 4-nitrophenyl phosphate, ATP, glucose-6-phosphate, and glycerol-3-phosphate. Phosphate detection by ammonium heptamolybdate reagent
-
-
?
additional information
?
-
-
less than 5% of the activity with myo-inositol hexakisphosphate with: ATP, ADP, glycerophosphate, glucose 1-phosphate, glucose 6-phosphate, fructose 6-phosphate and mannose 6-phosphate
-
?
additional information
?
-
-
less than 5% of the activity with myo-inositol hexakisphosphate with: ATP, ADP, glycerophosphate, glucose 1-phosphate, glucose 6-phosphate, fructose 6-phosphate and mannose 6-phosphate
-
?
additional information
?
-
-
hydrolysis of insoluble metal-phytates, overview. The enzyme is also active with 4-nitrophenyl phosphate, sodium diphosphate, glucose-1-phosphate, and glucose-6-phosphate
-
-
?
additional information
?
-
-
highest activity under anaerobic conditions, during the exponential growth no activity observed
-
-
?
additional information
?
-
-
undegraded phytates can cause mineral deficiencies in humans. The presence of undigested phytate in the colon may protect against the development of colonic carcinoma
-
-
?
additional information
?
-
the enzyme also shows phosphate-monoester phosphohydrolase activity, EC 3.1.3.2
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
-
the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate
-
-
?
additional information
?
-
-
the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate
-
-
?
additional information
?
-
substrate specificity of the recombinant isozyme, overview
-
-
?
additional information
?
-
substrate specificity of the recombinant isozyme, overview
-
-
?
additional information
?
-
-
determination of phytase activity of bacteriocins producing lactic acid bacteria previously isolated from spontaneous rye sourdough. The results show that the highest extracellular phytase activity produces Pediococcus pentosaceus KTU05-8 and KTU05-9 strains, as compared to Lactobacillus sakei strain KTU05-6, Pediococcus acidilactici strain KTU05-7, and Pediococcus pentosaceus KTU05-10, with a volumetric phytase activity of 32 and 54 U/ml, respectively, under conditions similar to leavening of bread dough (pH 5.5 and 30°C). In vitro studies in simulated gastrointestinal tract media pH provide that bioproducts prepared with Pediococcus pentosaceus strains used in wholemeal wheat bread preparation increase solubility of iron, zinc, manganese, calcium, and phosphorus average 30%
-
-
?
additional information
?
-
-
the enzyme catalyzes phosphate release from cereals such as corn, soybean, and wheat
-
-
?
additional information
?
-
-
the enzyme catalyzes phosphate release from cereals such as corn, soybean, and wheat
-
-
?
additional information
?
-
among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate
-
-
?
additional information
?
-
-
among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate
-
-
?
additional information
?
-
enzyme PhyA efficiently releases phosphate from feedstuffs such as soybean, rich bran, and corn meal. The enzyme shows significant substrate specificity for phytate and only low activity with 4-nitrophenyl phosphate, diphosphate, 2-naphthyl phosphate, alpha-glyceryl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1-phosphate, fructose 6-phosphate, AMP, ADP, and ATP
-
-
?
additional information
?
-
-
enzyme PhyA efficiently releases phosphate from feedstuffs such as soybean, rich bran, and corn meal. The enzyme shows significant substrate specificity for phytate and only low activity with 4-nitrophenyl phosphate, diphosphate, 2-naphthyl phosphate, alpha-glyceryl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1-phosphate, fructose 6-phosphate, AMP, ADP, and ATP
-
-
?
additional information
?
-
enzyme PhyA efficiently releases phosphate from feedstuffs such as soybean, rich bran, and corn meal. The enzyme shows significant substrate specificity for phytate and only low activity with 4-nitrophenyl phosphate, diphosphate, 2-naphthyl phosphate, alpha-glyceryl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1-phosphate, fructose 6-phosphate, AMP, ADP, and ATP
-
-
?
additional information
?
-
among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate
-
-
?
additional information
?
-
-
no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate
-
-
?
additional information
?
-
-
no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate
-
-
?
additional information
?
-
-
color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination
-
-
?
additional information
?
-
-
color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination
-
-
?
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
additional information
?
-
-
enzyme hydrolyzes phytate, the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
additional information
?
-
-
enzyme hydrolyzes phytate, the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
additional information
?
-
the enzyme shows no or poor activity with ATP, ADP, 4-nitrophenyl phosphate, diphosphate, glucose 6-phosphate, and fructose 6-phosphate
-
-
?
additional information
?
-
-
lower activity with 4-nitrophenyl phosphate, no or poor activity with AMP, ADP, ATP, GTP, NADP+, glucose 1-phosphate, and glucose 6-phosphate
-
-
?
additional information
?
-
-
role of phytase in Ca2+ mobilization during germination of mung bean seed via a salvage pathway that involves allosteric activation by myo-inositol triphosphate
-
?
additional information
?
-
-
no cleavage of myo-inositol 2-phosphate, 1,2-cyclic inositol phosphate, Na-3-glycerophosphate
-
-
?
additional information
?
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
?
additional information
?
-
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
?
additional information
?
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
?
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0.157 - 2
1-naphthyl phosphate
0.667 - 0.881
2-glycerophosphate
0.15 - 0.653
2-naphthyl phosphate
0.123 - 4.3
4-nitrophenyl phosphate
0.229 - 1.1
D-fructose 1,6-diphosphate
0.478 - 0.676
D-fructose 6-phosphate
0.302 - 2.3
D-glucose 6-phosphate
1.2
D-ribose 5-phosphate
-
-
0.105 - 0.812
diphosphate
0.09
fructose 1,6-diphosphate
-
-
0.045
fructose 6-phosphate
-
-
0.067
glucose 6-phosphate
-
-
0.075
Glycerol 2-phosphate
-
-
0.00098 - 6.7
myo-inositol hexakisphosphate
0.133
myo-inositol pentakisphosphate
-
-
0.25
myo-inositol trikisphosphate
-
-
0.054 - 0.67
myo-inositol-1,2,3,4,5,6-hexakisphosphate
0.093
O-phospho-L-Ser
-
-
0.74 - 11
O-phospho-L-serine
0.132 - 7.78
p-nitrophenyl phosphate
0.045 - 0.915
pyridoxal phosphate
additional information
additional information
-
0.157
1-naphthyl phosphate
-
-
0.49 - 2
1-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP2
0.516
1-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP11
0.718
1-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP12
1.6
1-naphthyl phosphate
-
-
0.667
2-glycerophosphate
-
pH 5.0, 35°C, phytase LP11
0.704
2-glycerophosphate
-
pH 5.0, 35°C, phytase LP2
0.881
2-glycerophosphate
-
pH 5.0, 35°C, phytase LP12
0.15
2-naphthyl phosphate
-
-
0.512
2-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP2
0.634
2-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP12
0.653
2-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP11
0.123
4-nitrophenyl phosphate
-
pH 5.0, 35°C, phytase LP12
0.152
4-nitrophenyl phosphate
-
pH 5.0, 35°C, phytase LP11
0.176
4-nitrophenyl phosphate
-
pH 5.0, 35°C, phytase LP2
1.38
4-nitrophenyl phosphate
-
pH 2.5
2.2
4-nitrophenyl phosphate
-
pH 5.6
4.3
4-nitrophenyl phosphate
-
-
0.142
ADP
-
-
0.398
ADP
-
pH 5.0, 35°C, phytase LP12
0.403
ADP
-
pH 5.0, 35°C, phytase LP11
0.451
ADP
-
pH 5.0, 35°C, phytase LP2
0.115
AMP
-
-
0.315
AMP
-
pH 5.0, 35°C, phytase LP12
0.319
AMP
-
pH 5.0, 35°C, phytase LP2
0.365
AMP
-
pH 5.0, 35°C, phytase LP11
0.145
ATP
-
-
0.412
ATP
-
pH 5.0, 35°C, phytase LP12
0.531
ATP
-
pH 5.0, 35°C, phytase LP11
0.596
ATP
-
pH 5.0, 35°C, phytase LP2
0.229
D-fructose 1,6-diphosphate
-
pH 5.0, 35°C, phytase LP11
0.359
D-fructose 1,6-diphosphate
-
pH 5.0, 35°C, phytase LP2
0.731
D-fructose 1,6-diphosphate
-
pH 5.0, 35°C, phytase LP12
1.1
D-fructose 1,6-diphosphate
-
-
0.478
D-fructose 6-phosphate
-
pH 5.0, 35°C, phytase LP11
0.531
D-fructose 6-phosphate
-
pH 5.0, 35°C, phytase LP2
0.676
D-fructose 6-phosphate
-
pH 5.0, 35°C, phytase LP12
0.302
D-glucose 6-phosphate
-
pH 5.0, 35°C, phytase LP2
0.401
D-glucose 6-phosphate
-
pH 5.0, 35°C, phytase LP11
0.634
D-glucose 6-phosphate
-
pH 5.0, 35°C, phytase LP12
2.3
D-glucose 6-phosphate
-
-
0.105
diphosphate
-
-
0.445
diphosphate
-
pH 5.0, 35°C, phytase LP11
0.691
diphosphate
-
pH 5.0, 35°C, phytase LP12
0.812
diphosphate
-
pH 5.0, 35°C, phytase LP2
0.153
GTP
-
-
0.217
GTP
-
pH 5.0, 35°C, phytase LP2
0.398
GTP
-
pH 5.0, 35°C, phytase LP11
0.423
GTP
-
pH 5.0, 35°C, phytase LP12
0.00098
myo-inositol hexakisphosphate
-
-
0.0072
myo-inositol hexakisphosphate
-
-
0.0104
myo-inositol hexakisphosphate
-
pH 5.5
0.016
myo-inositol hexakisphosphate
-
-
0.016
myo-inositol hexakisphosphate
-
in 0.1 M sodium acetate buffer, pH 4.5, at 37°C
0.017
myo-inositol hexakisphosphate
-
-
0.017
myo-inositol hexakisphosphate
-
in presence of Ca2+
0.018
myo-inositol hexakisphosphate
-
-
0.01945
myo-inositol hexakisphosphate
pH 5.0, 37°C, recombinant wild-type enzyme, substrate is sodium phytate
0.024
myo-inositol hexakisphosphate
-
isoenzyme with isoelectric point of 4.8
0.025
myo-inositol hexakisphosphate
-
isoenzyme with isoelectric point of 4.9
0.027
myo-inositol hexakisphosphate
-
pH 5.0, 58°C, native enzyme
0.03
myo-inositol hexakisphosphate
-
-
0.03
myo-inositol hexakisphosphate
-
-
0.03
myo-inositol hexakisphosphate
-
pH 5.0, 58°C
0.0318
myo-inositol hexakisphosphate
mutant D144N/V227A/G344D
0.033
myo-inositol hexakisphosphate
-
-
0.033
myo-inositol hexakisphosphate
-
pH 5.0, no salt
0.036
myo-inositol hexakisphosphate
-
pH 4.0, no salt
0.038
myo-inositol hexakisphosphate
-
-
0.0386
myo-inositol hexakisphosphate
-
mutant enzyme E228K, in 0.2 M citrate buffer at pH 5.5 and 37°C
0.04
myo-inositol hexakisphosphate
-
-
0.04
myo-inositol hexakisphosphate
strain NRRL 3135
0.04
myo-inositol hexakisphosphate
-
pH 5.0, 58°C
0.043
myo-inositol hexakisphosphate
-
isoenzyme with isoelectric point of 5.0
0.04875
myo-inositol hexakisphosphate
mutant D144N/V227A
0.05
myo-inositol hexakisphosphate
-
pH 7.0
0.05
myo-inositol hexakisphosphate
-
pH 5.0, 58°C, recombinant enzyme
0.057
myo-inositol hexakisphosphate
-
pH 4.0, 0.5 M NaCl
0.061
myo-inositol hexakisphosphate
-
-
0.072
myo-inositol hexakisphosphate
pH 2.5, no salt
0.08
myo-inositol hexakisphosphate
-
pH 5.0, 35°C, phytase LP11
0.08
myo-inositol hexakisphosphate
phytic acid dipotassium salt
0.088
myo-inositol hexakisphosphate
-
pH 5.5, 0.5 M NaCl
0.09
myo-inositol hexakisphosphate
-
mutant enzyme E272K, in 0.2 M glycine-HCl, at pH 3.2
0.1
myo-inositol hexakisphosphate
-
-
0.11
myo-inositol hexakisphosphate
-
-
0.117
myo-inositol hexakisphosphate
-
-
0.12
myo-inositol hexakisphosphate
-
-
0.121
myo-inositol hexakisphosphate
pH 2.5, 0.5 M NaCl
0.1235
myo-inositol hexakisphosphate
wild-type
0.124
myo-inositol hexakisphosphate
-
pH 5.0, 58°C, recombinant enzyme
0.13
myo-inositol hexakisphosphate
-
-
0.13
myo-inositol hexakisphosphate
-
pH 5.0, 35°C, phytase LP2
0.13
myo-inositol hexakisphosphate
-
mutant enzyme E272K, in 0.2 M glycine-HCl, at pH 2.5
0.135
myo-inositol hexakisphosphate
-
-
0.14
myo-inositol hexakisphosphate
phytic acid sodium salt
0.15
myo-inositol hexakisphosphate
-
-
0.15
myo-inositol hexakisphosphate
phytic acid sodium salt
0.156
myo-inositol hexakisphosphate
-
Vmax: 83 nmol/mg/s
0.16
myo-inositol hexakisphosphate
-
pH 5.0
0.16
myo-inositol hexakisphosphate
phytic acid dipotassium salt
0.17
myo-inositol hexakisphosphate
Vmax: 1714 micromol/min/mg
0.1773
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M citrate buffer at pH 5.5 and 37°C
0.18
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli
0.186
myo-inositol hexakisphosphate
-
in 0.1 M sodium acetate buffer, pH 6.0, at 37°C
0.196
myo-inositol hexakisphosphate
-
0.2
myo-inositol hexakisphosphate
-
-
0.2
myo-inositol hexakisphosphate
pH 6.0, no salt
0.206
myo-inositol hexakisphosphate
-
0.21
myo-inositol hexakisphosphate
-
pH 2.5, 60°C
0.22
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris
0.2278
myo-inositol hexakisphosphate
-
mutant enzyme E228K, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C
0.24
myo-inositol hexakisphosphate
recombinant protein
0.246
myo-inositol hexakisphosphate
-
-
0.247
myo-inositol hexakisphosphate
-
pH 5.0, 37°C
0.25
myo-inositol hexakisphosphate
-
-
0.25
myo-inositol hexakisphosphate
-
-
0.25
myo-inositol hexakisphosphate
-
isoenzyme II
0.26
myo-inositol hexakisphosphate
-
-
0.27
myo-inositol hexakisphosphate
-
phytase 2
0.3
myo-inositol hexakisphosphate
-
-
0.3
myo-inositol hexakisphosphate
-
pH 5.0, 35°C, phytase LP12
0.3
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Schizosaccharomyces pombe. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.32
myo-inositol hexakisphosphate
-
sodium phytate, pH 5.0, 60°C
0.3219
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C
0.33
myo-inositol hexakisphosphate
-
-
0.334
myo-inositol hexakisphosphate
-
-
0.36
myo-inositol hexakisphosphate
-
-
0.36
myo-inositol hexakisphosphate
-
isoenzyme I
0.37
myo-inositol hexakisphosphate
-
phytase 1
0.38
myo-inositol hexakisphosphate
-
pH 5.5, 40°C
0.382
myo-inositol hexakisphosphate
-
recombinant wild-type enzyme, pH 2.5, 40°C
0.392
myo-inositol hexakisphosphate
-
0.4
myo-inositol hexakisphosphate
-
-
0.405
myo-inositol hexakisphosphate
-
recombinant mutant enzyme, pH 2.5, 40°C
0.42
myo-inositol hexakisphosphate
pH 4.5, 50°C
0.44
myo-inositol hexakisphosphate
strain 92
0.46
myo-inositol hexakisphosphate
-
pH 4, 37°C
0.48 - 0.545
myo-inositol hexakisphosphate
pH 5.5, 55°C, sodium phytate
0.51
myo-inositol hexakisphosphate
-
pH 2.0, 37°C, recombinant enzyme
0.52
myo-inositol hexakisphosphate
-
0.532
myo-inositol hexakisphosphate
native protein
0.54
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M glycine-HCl, at pH 3.2
0.545
myo-inositol hexakisphosphate
pH 4.5, 55°C
0.55
myo-inositol hexakisphosphate
-
-
0.606
myo-inositol hexakisphosphate
-
pH 2.5, 55°C. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.625
myo-inositol hexakisphosphate
-
at 55°C, pH 2.5
0.65
myo-inositol hexakisphosphate
-
-
0.7
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Pichia pastoris (pPICZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.757
myo-inositol hexakisphosphate
pH 5.0, 55°C
0.77
myo-inositol hexakisphosphate
-
mutant enzyme E272Q, in 0.2 M glycine-HCl, at pH 3.2
0.8
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Pichia pastoris (pGAPZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.83
myo-inositol hexakisphosphate
-
-
1
myo-inositol hexakisphosphate
recombinant enzyme, in 0.1 M sodium acetate buffer (pH 4.5) at 37°C
1.2
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Saccharomyces cerevisiae. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
1.5
myo-inositol hexakisphosphate
-
phytase II
1.5
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Schizosaccharomyces pombe. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
1.8
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Pichia pastoris (pGAPZalphaA) or Pichia pastoris (pPICZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
2.1
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Saccharomyces cerevisiae. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
2.2
myo-inositol hexakisphosphate
-
phytase IC
2.4
myo-inositol hexakisphosphate
-
-
2.8
myo-inositol hexakisphosphate
-
phytase IB
2.84
myo-inositol hexakisphosphate
-
pH 5.5
4.5
myo-inositol hexakisphosphate
-
phytase ID
4.72
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M glycine-HCl, at pH 2.5
4.79
myo-inositol hexakisphosphate
-
mutant enzyme E272Q, in 0.2 M glycine-HCl, at pH 2.5
6.7
myo-inositol hexakisphosphate
-
phytase IA
0.054
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b, pH 5.0, 36°C
0.35
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant wild-type enzyme, pH 4.5, 37°C
0.36
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73S, pH 4.5, 37°C
0.53
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73D, pH 4.5, 37°C
0.61
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73E, pH 4.5, 37°C
0.67
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73T, pH 4.5, 37°C
0.74
O-phospho-L-serine
-
pH 5.0, 35°C, phytase LP12
0.8 - 11
O-phospho-L-serine
-
pH 5.0, 35°C, phytase LP2
0.891
O-phospho-L-serine
-
pH 5.0, 35°C, phytase LP11
0.132
p-nitrophenyl phosphate
-
-
0.555
p-nitrophenyl phosphate
-
-
7.78
p-nitrophenyl phosphate
-
-
0.138
phytate
-
wild-type enzyme
0.747
phytate
-
mutant enzyme E227A
0.914
phytate
-
mutant enzyme D55A
0.934
phytate
-
mutant enzyme Y159H
0.967
phytate
-
mutant enzyme K76E
2.505
phytate
-
mutant enzyme R122E
3.046
phytate
-
mutant enzyme R122K
3.542
phytate
-
mutant enzyme D258A
8.661
phytate
-
mutant enzyme Y159A
11.99
phytate
-
mutant enzyme K76R
0.045
pyridoxal phosphate
-
-
0.776
pyridoxal phosphate
-
pH 5.0, 35°C, phytase LP11
0.876
pyridoxal phosphate
-
pH 5.0, 35°C, phytase LP12
0.915
pyridoxal phosphate
-
pH 5.0, 35°C, phytase LP2
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
-
Lineweaver-Burk plots
-
additional information
additional information
Line-Weaver Burk plot
-
additional information
additional information
-
Line-Weaver Burk plot
-
additional information
additional information
Michaelis-Menten kinetics and Lineweaver-Burk plots
-
additional information
additional information
-
Michaelis-Menten kinetics and Lineweaver-Burk plots
-
additional information
additional information
-
Michealis-Menten kinetics
-
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-
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified. Growth and phosphorus nutrition of the plants supplied with phytate is improved significantly when the phytase gene from Aspergillus niger is introduced. The Aspergillus phytase is only effective when secreted as an extracellular enzyme by inclusion of the signal peptide sequence from the carrot extensin gene
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
var. awamorii ATCC 38854. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
BCC18313 (TR86), the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
UniProt
brenda
-
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Aspergillus syndowi
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
cv Sang
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate; the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
UniProt
brenda
isolated from Lake Kasumigaura, Japan
UniProt
brenda
isolated from Lake Kasumigaura, Japan
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from a rhizosphere
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
strainMO-3. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from Lor cheese samples
-
-
brenda
isolated from Lor cheese samples
-
-
brenda
var. amiga. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isozyme b; isozyme b
UniProt
brenda
isozyme b; isozyme b
UniProt
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate; DSMZ 18074, the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
UniProt
brenda
strains KTU05-8 and KTU05-9, isolated from spontaneous Lithuanian rye sourdoughs
-
-
brenda
Penicillium caseoicolum
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Bacteroides ruminicola, isolated from Mehsani buffalo rumen
UniProt
brenda
isolated from chickpea (Cicer arietinum) rhizosphere
-
-
brenda
isolated from chickpea (Cicer arietinum) rhizosphere
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from Antarctic deep-sea sediment
-
-
brenda
isolated from Antarctic deep-sea sediment
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Schwanniomyces castellii
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
fragment; strain ATCC 49690
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
-
-
-
brenda
isolated from wheat rhizosphere
UniProt
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
ATCC 130703. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
-
-
-
brenda
ATCC 9142. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
BCC18081 (TR170), the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
UniProt
brenda
NRRL 3135. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
strain 92 and strain NRRL 3135. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissPRot
brenda
strain NRRL3135. The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme exhibits phytase and acid phosphatase activity. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified. Growth and phosphorus nutrition of the plants supplied with phytate is improved significantly when the phytase gene from Aspergillus niger is introduced.The Aspergillus phytase is only effective when secreted as an extracellular enzyme by inclusion of the signal peptide sequence from the carrot extensin gene
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
van Teighem
-
-
brenda
van Teighem. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
strain NRRL3135. The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
-
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate; the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
-
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
UniProt
brenda
calf
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
2 isoenzymes
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
var. toria
-
-
brenda
multiple forms: phytase IA, IB, IC, ID and II
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
expressed in Saccharomyces cerevisiae
-
-
brenda
gene APPA
UniProt
brenda
K12 ATCC 33965
-
-
brenda
recombinantly expressed in Saccharomyces cerevisiae, Pichia pastoris or Pseudomonas fluorescens
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
UniProt
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
UniProt
brenda
-
SwissProt
brenda
L. Merr.. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
L.cv. Himalaya
-
-
brenda
subsp. vulgare
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Thunb. Cv. Nellie White, 2 enzyme forms pH 5 phytase and pH 8 phytase
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
SwissProt
brenda
-
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
ATCC 22959. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SWissProt
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
-
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from a soil metagenome
-
-
brenda
metagenome-derived phytase, metagenome derived from subsurface groundwater
-
-
brenda
minor
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
strain cv B-1
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
L. var. Consul, 3 isoenzymes with isolelectric points of 5.0, 4.9, and 4.8
-
-
brenda
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G277K
-
mutation increases the activity of the enzyme at pH 2.8-3.4. Mutation decreases the relative activity at pH values of above 6.3
K68A
-
mutation decreases the pH optimum with phytate as substrate by 0.5 to 1.0 unit, with either no change or even a slight increase in maximum specific activity
Q27A
-
1.1fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. The pH-activity profile resembles that of wild-type enzyme with slight increases below pH 4.0 and around pH 6.5
Q27G
-
2.3fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme.Increase in specific activity is almost constant over entire pH-range, pH 4-8
Q27I
-
3.1fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Remarkable increase in specific activity around pH 6.5, while having no or only a modest effect in the more acidic pH range. The shape of the pH-profile strongly resembles that of Aspergillus terreus - which also has Leu at postion 27
Q27N
-
1.7fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Increase in specific activity is almost constant over entire pH-range, pH 4-8
Q27P
-
1.7fold decrease in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Mutant enzyme has a pronounced tendency to aggregate and precipitate
Q27S
-
1.9fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme
Q27T
-
2.8fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Increase in specific activity over the entire pH-range, pH 4-8
Q27V
-
1.3fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme
S140Y/D141G
-
mutation decreases the pH optimum with phytate as substrate by 0.5 to 1.0 unit, with either no change or even a slight increase in maximum specific activity
Y282H
-
mutation increases the activity of the enzyme at pH 2.8-3.4. Mutation decreases the relative activity at pH values of above 6.3
D262H
-
increased activity compared to the wild type enzyme
E228K
-
shows a shift of the pH optimum to 3.8 and 266% greater hydrolysis of soy phytate at pH 3.5 than the wild type enzyme
E228K/K300R/K301E
-
shows large increase in the phytase activity ratio at pH 3.5 over pH 5.5
E228Q
-
decreased activity compared to the wild type enzyme
E272K
-
activity optimum at pH 3.2, shows improvement in substrate affinity
E272Q
-
pH optimum similar to the wild type enzyme
E89D
-
mutant enzyme from strain T213, slight decrease in activity
E89D/H292N/R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
E89D/R297Q
-
mutant enzyme from strain T213, 2.6fold increase in activity
H292N
-
mutant enzyme from strain T213, as active as wild-type enzyme
H292N/R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
K300D
-
specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.71
K300E
-
mutation results in an increase of the hydrolysis of phythic acid of 56% and 19% at pH 4.0 and pH 5.0 at 37°C respectively. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.74
K300E/K301E
-
greater improvement in relative activity at pH 3.5 and lower specific activity than the wild type enzyme
K300R
-
specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.81
K300T
-
specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.68
K301E
-
increased activity compared to the wild type enzyme
K91A
-
decreased activity compared to the wild type enzyme
K91E
-
increased activity compared to the wild type enzyme
K94E
-
decreased activity compared to the wild type enzyme
K94E/K300E/K301E
-
greater improvement in relative activity at pH 3.5 and lower specific activity than the wild type enzyme
Q50L
-
increased activity compared to the wild type enzyme
Q50P
-
increased activity compared to the wild type enzyme
R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
E272K
-
activity optimum at pH 3.2, shows improvement in substrate affinity
-
E272Q
-
pH optimum similar to the wild type enzyme
-
E89D
-
mutant enzyme from strain T213, slight decrease in activity
-
E89D/R297Q
-
mutant enzyme from strain T213, 2.6fold increase in activity
-
H292N
-
mutant enzyme from strain T213, as active as wild-type enzyme
-
H292N/R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
-
R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
-
E89D
-
mutant enzyme from strain T213, slight decrease in activity
-
E89D/R297Q
-
mutant enzyme from strain T213, 2.6fold increase in activity
-
H292N
-
mutant enzyme from strain T213, as active as wild-type enzyme
-
H292N/R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
-
R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
-
A68S/A72E/A73E/S77N
-
t1/2 at 49°C decreases from 53 min for the wild-type enzyme to 20 min for the mutant enzyme
E41A/D42G
-
t1/2 at 49°C increases from 53 min for the wild-type enzyme to 76 min for the mutant enzyme
H61E
-
t1/2 at 49°C increases from 53 min for the wild-type enzyme to 54 min for the mutant enzyme
A68S/A72E/A73E/S77N
-
t1/2 at 49°C decreases from 53 min for the wild-type enzyme to 20 min for the mutant enzyme
-
E41A/D42G
-
t1/2 at 49°C increases from 53 min for the wild-type enzyme to 76 min for the mutant enzyme
-
H61E
-
t1/2 at 49°C increases from 53 min for the wild-type enzyme to 54 min for the mutant enzyme
-
D258A
-
turnover number of mutant enzyme is 20.87% of that of the wild-type enzyme
D314A
-
inactive mutant enzyme
D55A
-
turnover number of mutant enzyme is 0.21% of that of the wild-type enzyme
E211A
-
inactive mutant enzyme
E227A
-
turnover number of mutant enzyme is 9.29% of that of the wild-type enzyme
E260A
-
inactive mutant enzyme
K76E
-
turnover number of mutant enzyme is 0.26% of that of the wild-type enzyme
K76R
-
turnover number of mutant enzyme is 0.3% of that of the wild-type enzyme
R122E
-
turnover number of mutant enzyme is 48.81% of that of the wild-type enzyme
R122K
-
turnover number of mutant enzyme is 17.11% of that of the wild-type enzyme
Y159F
-
inactive mutant enzyme
D55A
-
turnover number of mutant enzyme is 0.21% of that of the wild-type enzyme
-
E260A
-
inactive mutant enzyme
-
K76E
-
turnover number of mutant enzyme is 0.26% of that of the wild-type enzyme
-
K76R
-
turnover number of mutant enzyme is 0.3% of that of the wild-type enzyme
-
Y159F
-
inactive mutant enzyme
-
D144N/V227A
38% higher specific activity than wild-type, lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type, Km (myo-inositol hexakisphosphate) lower compared to wild-type, kcat similar to wild-type
D144N/V227A/G344D
mutant releases 25% more inorganic phosphorus from soy phytate than the wild-type enzyme, mutant shows higher thermostability compared to wild-type, Km (myo-inositol hexakisphosphate) lower compared to wild-type, kcat similar to wild-type
D144N/V227A/G344D/D112N
7% higher specific activity than wild-type, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/D112N/K46E
lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/D112N/K46E/G103S
lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/D112N/K46E/G103S/S209G
23% higher specific activity than wild-type, lower efficiency for soy phytate hydrolysis compared to wild-type enzyme
D144N/V227A/G344D/K46E
similar efficiency for soy phytate hydrolysis as compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/K65E
lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
G73D
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73E
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73L
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73R
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73S
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73T
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73Y
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
-
highly active phytase with no loss of activity after heating at 62°C for 1 h and 27% of its initial activity after 10 min at 85°C, which is a significant improvement over the appA parental phytase. The mutant enzyme also shows a 3.5fold enhancement in gastric stability
S392F
site-directed mutagenesis, three-dimensional structure analysis, modeling, and comparison to wild-type structure. The mutant phytase shows 12.8%, 9.6% and 10.3% higher phytase activity at pH 6, 7 and 8, respectively, compared to wild-type enzyme, and the mutant enzymes shows thermostability improvement of 74% and 78.4% at 80°C and 90°C, respectively, compared to wild-type
T308A
5% of the specific activity of wild-type
T101C/A229C/S307C/V352C/M364C/F398C
-
enhancing the thermal resistance of the acidobacteria-derived phytase by engineering of disulfide bridges, construction of engineered mutant rPhyA6DB by site-directed mutagenesis, overview
E153R
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230A
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230D
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230K
site-directed mutagenesis, the mutant shows reduced catalytic activity and thermal stability compared to the wild-type enzyme
E230P
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230S
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230T
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162A
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162V
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A/L162G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A/L162G/L230G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
V162L
site-directed mutagenesis, the mutant shows increased sensitivity to pepsin in contrast to the less sensitive wild-type enzyme
Q27L
-
3.4fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Remarkable increase in specific activity around pH 6.5, while having no or only a modest effect in the more acidic pH range. The shape of the pH-profile strongly resembles that of Aspergillus terreus - which also has Leu at postion 27
Q27L
-
mutation increases the specific activity mainly around pH 6.5, while the increase is much smaller in the pH range 2 to 5, the pH that seems most relevant for maximal performance of the enzyme in animals. Decreasing the negative surface charge of the Aspergillus fumigatus Q27L phytase mutant by glycinamidylation of the surface carboxy groups (of Asp and Glu residues) lowers the pH-optimum by ca. 0.5 unit but also results in 70-75% inactivation of the enzyme
Y159A
-
turnover number of mutant enzyme is 0.19% of that of the wild-type enzyme
Y159A
-
turnover number of mutant enzyme is 0.37% of that of the wild-type enzyme
additional information
-
replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme
additional information
-
replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme
-
additional information
construction of gene disruption null mutants of orf19.3727 of both chromosomal copies by PCR-based gene targeting method, PCR using gene-specific primers and plasmids pFA-ARG4 or pFA-HIS1. The ura3 auxotrophy in the null mutants was recovered by integrating plasmid CIp10 (carries URA3) into the RPS10 locus. Candida albicans orf19.3727 reintegrants are created by transforming full-length orf19.3727 into the null mutants. Phenotypes, overview
additional information
-
construction of gene disruption null mutants of orf19.3727 of both chromosomal copies by PCR-based gene targeting method, PCR using gene-specific primers and plasmids pFA-ARG4 or pFA-HIS1. The ura3 auxotrophy in the null mutants was recovered by integrating plasmid CIp10 (carries URA3) into the RPS10 locus. Candida albicans orf19.3727 reintegrants are created by transforming full-length orf19.3727 into the null mutants. Phenotypes, overview
additional information
-
construction of gene disruption null mutants of orf19.3727 of both chromosomal copies by PCR-based gene targeting method, PCR using gene-specific primers and plasmids pFA-ARG4 or pFA-HIS1. The ura3 auxotrophy in the null mutants was recovered by integrating plasmid CIp10 (carries URA3) into the RPS10 locus. Candida albicans orf19.3727 reintegrants are created by transforming full-length orf19.3727 into the null mutants. Phenotypes, overview
-
additional information
no further improvement in thermostability is observed by adding other mutations to D144N/V227A/G344D, which might result from unfavorable electrostatic interactions or structural perturbation
additional information
-
no further improvement in thermostability is observed by adding other mutations to D144N/V227A/G344D, which might result from unfavorable electrostatic interactions or structural perturbation
additional information
the HvPAPhy_a-transformed barley plants with high phytase activities possess triple potential utilities for the improvement of phosphate bioavailability. First of all, the utilization of the mature grains as feed to increase the release of bio-available phosphate and minerals bound to the phytate of the grains, secondly, the utilization of the powdered straw either directly or phytase extracted hereof as a supplement to high phytate feed or food, and finally, the use of the stubble to be ploughed into the soil for mobilizing phytatebound phosphate for plant growth
additional information
-
mutations of genes grrA and grrS, encoding GacA/GacS-like 2-component global regulatory system, or in gene rpoS encoding the sigma factor RpoS subunit of RNA polymerase, leads to a deficiency in phytase production. Introduction into mutants of the respective wild-type genes cloned into the wide-range plasmid pJFF224-NX under the control of the bacteriophage T4 gene 32 promoter complements this deficiency
additional information
-
mutations of genes grrA and grrS, encoding GacA/GacS-like 2-component global regulatory system, or in gene rpoS encoding the sigma factor RpoS subunit of RNA polymerase, leads to a deficiency in phytase production. Introduction into mutants of the respective wild-type genes cloned into the wide-range plasmid pJFF224-NX under the control of the bacteriophage T4 gene 32 promoter complements this deficiency
-
additional information
engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview
additional information
-
engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview
additional information
engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview
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0 - 15
purified recombinant His-tagged enzyme, over 50% activity remaining
10 - 50
-
purified enzyme, 30 min, pH 6.5, in presence of 20 mM Ca2+, completely stable, 40% activity is retained at 10°C. The enzyme is more thermostable in presence of CaCl2 and exhibits almost 100% residual activity at temperature range 20-50°C and 63% activity at 70°C after 30 min of preincubation, followed by sharp decline in thermostability
10 - 80
-
purified native enzyme, over 70% activity remains after 180 h
30
-
24 h, stable. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
30 - 50
-
1 h, no loss of activity
40 - 55
-
10 min, no loss of activity
45 - 50
-
there are two phases in thermal inactivation: when the temperature is between 45°C and 50°C, the thermal inactivation can be characterized as an irreversible inactivation which has some residual activity and when the temperature is above 55°C the thermal inactivation can be characterized as an irreversible process which has no residual activity
48
-
melting temperature, recombinant His-tagged enzyme
50 - 75
-
the purified phytase retains 73.6% of its activity after being incubated at 50°C for 10 min, while its activity is quickly lost after incubation at 65°C or 70°C for 10 min
50 - 80
-
half-life of the enzyme at 50, 60, 70 and 80°C is 866.2, 693.0, 37.8 and 11.3 min, respectively. The activity is lost completely at 80°C after 55 min incubation
60 - 80
enzyme activity is above 60% after treatment at 80°C for 10 min, and 54% of the activity is retained at 80°C for 15 min
62
-
1 h, no loss of activity, mutant enzyme Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
64
-
Tm-value for parental phytase is 63.7°C
66.5
thermic denaturation (1 h)
75.7
-
Tm-value for mutant enzyme Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
100
-
a minor increase of wild type enzyme activity is observed after 1 min, after 5 and 20 min at 100°C the activity is reduced to 4% and 1% of the initial activity
100
-
purified recombinant enzyme, pH 2.0, after 20 min inactivation, loss of 50% activity after 4 min
100
-
15 min, complete inactivation
37
-
20 min, less than 5% of activity of enzyme in 0.01 M sodium citrate buffer, about 5% loss of activity in 0.2 M sodium citrate buffer, about 10% loss of activity in 0.2 M sodium acetate buffer, about 15% loss of activity in 0.01 sodium acetate bugffer
37
-
24 h, stable. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
37
-
purified recombinant His-tagged wild-type enzyme, pH 2.5, half-life is 2 h, and for mutant rPhyA6DB 5.4 h
37
-
1 h, 90% loss of activity, 81-85% protection when heated in presence of myo-inositol hexakisphosphate, glucose 6-phosphate or phosphate
40
-
90 min, 15% loss of activity
40
-
90 min, no loss of activity up to
45
-
24 h, stable. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
45
-
90 min, no significant loss of activity at temperatures up ro, phytase LP11, LP12 and LP2
49
-
t1/2: 138 min, wild-type enzyme
49
-
t1/2: 53 min, wild-type enzyme
50
-
4°C, 90 min, 61% loss of activity
50
-
pH 4, 30 min, stable up to
50
-
10 min, stable up to
50
-
30 min, in presence of sodium myo-inositol hexakisphosphate or p-nitrophenyl phosphate, 1 mM Mg2+, 0.04 M Tris-succinate buffer, pH 7.0, less than 10% inactivation
50
-
90 min, 15% loss of activity of phytase, phytase LP11, LP12 and LP2
50
-
90 min, 15% loss of activity
55
-
there are two phases in thermal inactivation: when the temperature is between 45°C and 50°C, the thermal inactivation can be characterized as an irreversible inactivation which has some residual activity and when the temperature is above 55°C the thermal inactivation can be characterized as an irreversible process which has no residual activity
55
-
24 h, 11% loss of activity in absence of stabilizing agent, 7% loss of activity in presence of 10 mM CaCl2, 3% loss of activity in presence of 10 mM glycine. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
55
-
pH 4, 30 min, about 65% loss of activity
55
-
10 min, stable, recombinant enzyme from different expression systems. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
55
-
10 min, 25% loss of activity
60
-
1 min incubation at 60°C does not negatively affect the phytase activity of the wild type enzyme
60
-
4°C, 90 min, complete inactivation
60
-
10 min, in presence of 10 mM CaCl2, stable up to
60
-
pH 4, 30 min, about 90% loss of activity
60
-
60 min: 40% loss of activity of phytase IA, 30% loss of activity of phytase IB, 25% loss of activity of phytase IC, 30% loss of activity of phytase ID, 10% loss of activity of phytase II
60
-
1 h, 76% loss of activity
60
-
loses about 50% of the original activity after 1 h at 60°C
60
-
10 min, stable up to
60
-
10 min, 5% loss of activity
60
-
30 min, 70% inactivation
60
-
90 min, 90 min, 79% loss of activity of phytase LP22, 92% loss of activity of phytase LP12 and 85% loss of activity of phytase LP2
60
-
90 min, 20% loss of activity
60
-
purified recombinant enzyme, pH 2.0, after 30 min inactivation, loss of 50% activity after 15 min
60
-
purified recombinant His-tagged wild-type enzyme, pH 7.0, half-life is 5.2 min, and for mutant rPhyA6DB 14.5 min
65
-
20 min, about 35% loss of activity in 0.01 M sodium acetate buffer, about 40% loss of activity in 0.2 M acetate buffer, about 45% loss of activity in 0.01 M sodium citrate buffer, about 65% loss of activity in 0.2 M sodium citrate buffer
65
-
half-life: 30 min in absence of stabilizing agent, 6 h in presence of 20 mM glycine, 2 h in presence of 10 mM CaCl2. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
65
-
pH 4, 30 min, about 95% loss of activity
65
-
10 min, 55-70% loss of activity, recombinant enzyme from different expression systems. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
65
-
10 min, 55% loss of activity
65
-
10 min, 70% loss of activity
70
-
2 min, 42% loss of activity
70
-
2 min, 42% loss of activity, irreversible
70
10 min, about 15% loss of activity, in presence of 1 mM Ca2+
70
-
10 min, in presence of 10 mM CaCl2, 35% loss of activity
70
-
10 min, about 70% loss of activity, with 1 mM Ca2+
70
-
enzyme is stable up to 70°C
70
-
complete inactivation after 50 min
70
-
60 min: 65% loss of activity of phytase IA, 55% loss of activity of phytase IB, 60% loss of activity of phytase IC, 58% loss of activity of phytase ID, 40% loss of activity of phytase II
70
-
1 h, complete loss of activity
70
-
10 min, 90% loss of activity
70
-
10 min, about 50% loss of activity
70
-
10 min, 91% loss of activity
70
-
15 s, 90% loss of activity
70
-
80% activity at 70°C and pH 8.0 for up to 3 h
70
-
10 min, complete inactivation
75
10 min, about 35% loss of activity, in presence of 1 mM Ca2+
75
-
10 min, about 65% loss of activity, with 1 mM Ca2+
75
-
10 min, 10-20% loss of activity, recombinant enzyme from different expression systems. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
80
pH 5.5, 60 min,53% loss of activity
80
-
2 min, 92% loss of activity
80
-
2 min, 92% loss of activity, irreversible
80
-
3 min, 78% loss of activity
80
10 min, about 35% loss of activity, in presence of 1 mM Ca2+
80
-
10 min, in presence of 10 mM CaCl2, 50% loss of activity
80
-
about 50% of its original activity remains after incubation at 80°C for 10 min in the presence of 10 mM CaCl2
80
-
10 min, about 60% loss of activity, with 1 mM Ca2+
80
pH 5.5, 60 min, 62% loss of activity
80
pH 5.5, 60 min, 78% loss of activity
80
-
60 min: 90% loss of activity of phytase IA, 80% loss of activity of phytase IB, 92% loss of activity of phytase IC, 88% loss of activity of phytase ID, 80% loss of activity of phytase II
80
-
half-life is 11.3 min
80
-
10 min, complete loss of activity
80
pH 5.5, 60 min, 38% loss of activity
80
-
enzyme expressed from synthetic gene encoding Peniophora lycii phytase expressed in methylotrophic yeast Pichia pastoris, 75% loss of activity after 10 min
80
-
10 min, complete inactivation
80
-
about 25% loss of activity after 1 min, about 50% loss of activity after 2 min, about 65% loss of activity after 3 min
80
pH 5.5, 60 min, 85% loss of activity
80
-
purified recombinant enzyme, pH 2.0, after 25 min inactivation, loss of 50% activity after 7 min
80
-
purified recombinant His-tagged wild-type enzyme, pH 7.0, half-life is 2.3 min, and for mutant rPhyA6DB 7.0 min
80
-
15 min, 15% loss of activity
80
retains 14% activity at 80°C
80
retains 50% activity at 80°C
85
10 min, about 30% loss of activity, in presence of 1 mM Ca2+
85
-
10 min, about 45% loss of activity, with 1 mM Ca2+
85
-
10 min, 27% loss of activity,mutant enzyme Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
90
-
20 min, about 35% loss of activity in 0.01 M sodium acetate buffer, about 40% loss of activity in 0.2 M acetate buffer, about 45% loss of activity in 0.01 M sodium citrate buffer, about 65% loss of activity in 0.2 M sodium citrate buffer
90
10 min, about 30% loss of activity, in presence of 1 mM Ca2+
90
-
10 min, about 65% loss of activity, with 1 mM Ca2+
90
-
10 min, complete inactivation
95
about 40% loss of activity after 15 min, about 60% loss of activity after 30 min, in presence of 5 mM ca2+
95
-
about 55% loss of activity after 15 min, about 75% loss of activity after 30 min, with 5 mM Ca2+
additional information
more than 50% activity is retained after heating at 100°C for 10 min
additional information
more than 50% activity is retained after heating at 100°C for 10 min
additional information
-
replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme
additional information
-
phyL exhibits high thermal stability, even at a lower calcium concentration, as it is able to recover 80% of its original activity after denaturation at 95 °C for 10 min
additional information
the enzyme upon denaturation for 10 min at 75, 85 and 95°C, followed by 1 h renaturation at the room temperature (28°C) in the presence of 5 mmol/l Ca2+, restores 86%, 54%, and 37% activity
additional information
-
the enzyme upon denaturation for 10 min at 75, 85 and 95°C, followed by 1 h renaturation at the room temperature (28°C) in the presence of 5 mmol/l Ca2+, restores 86%, 54%, and 37% activity
additional information
in the presence CaCl2, PHY US417 recoveres 77% of its activity after incubation at 75°C for 10 min. In the absence of calcium, even so PHY US417 is absolutely stable when incubated for 30 min at 50°C it retains only 22% of activity after 10 min at 60°C
additional information
-
in the presence CaCl2, PHY US417 recoveres 77% of its activity after incubation at 75°C for 10 min. In the absence of calcium, even so PHY US417 is absolutely stable when incubated for 30 min at 50°C it retains only 22% of activity after 10 min at 60°C
additional information
enzyme retains stability when incubated at 50°C for 30 min, and over 70% activity retain. Enzyme loses activity rapidly at higher temperatures, with more than 90% activity lost after incubating at 70°C for 2 min
additional information
-
enzyme retains stability when incubated at 50°C for 30 min, and over 70% activity retain. Enzyme loses activity rapidly at higher temperatures, with more than 90% activity lost after incubating at 70°C for 2 min
additional information
-
T1/2 of 16 h at 60°C and 1.5 h at 80°C
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agriculture
-
a 20fold increase in total root phytase activity in transgenic lines expressing Aspergillus niger phytase results in improved phosphorus nutrition, such that the growth and phosphorus content of the plants is equivalent to control plants supplied with inorganic phosphate. Use of gene technology to improve the ability of plants to utilize accumulated forms of soil organic phosphorus
agriculture
-
a 20fold increase in total root phytase activity in transgenic lines expressing Aspergillus niger phytase results in improved phosphorus nutrition, such that the growth and phosphorus content of the plants is equivalent to control plants supplied with inorganic phosphate. Use of gene technology to improve the ability of plants to utilize accumulated forms of soil organic phosphorus
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
Schwanniomyces castellii
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
Penicillium caseoicolum
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
Aspergillus syndowi
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
enzyme is used in animal feed to reduce phosphate pollution
agriculture
-
since monogastric animals virtually lack phytase activity in their digestive tract, phytic acid phosphorus is metabolically unavailable to these animals. The problem can be circumvented by supplementation of the feed with a recombinantly produced phytase that has a pH activity profile ideally suited for maximal activity in the digestive tract of either pigs or poultry
agriculture
-
the enzyme is suitable for supplementing animal feeds to improve the availability of phosphate from phytate
agriculture
actopic expressing of phytase during seed development offers an effective strategy for improving phosphorus availability in seeds. The ability to reduce the amount of phytate in seed will improve nutrient availability for animal feed
agriculture
-
the ability of the enzyme to liberate phytate-phosphate is similar when included in low Ca2+ and nonphytate phosphorus diets for broilers. Either source can be fed to commercial broilers to aid improving phytate-bound phosphate use
agriculture
-
supplementation of phytases into the monogastric animals feed can reduce the phosphorus excretion and result in improved availability of trace elements, minerals, amino acids, and energy. The enzyme has great potential for feed applications, especially in aquaculture
agriculture
the RPHY1 gene mined from rumen proves its promising candidature as a feed supplement enzyme in animal farming
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
-
agriculture
-
supplementation of phytases into the monogastric animals feed can reduce the phosphorus excretion and result in improved availability of trace elements, minerals, amino acids, and energy. The enzyme has great potential for feed applications, especially in aquaculture
-
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
-
biotechnology
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a 20fold increase in total root phytase activity in transgenic lines expressing Aspergillus niger phytase results in improved phosphorus nutrition, such that the growth and phosphorus content of the plants is equivalent to control plants supplied with inorganic phosphate. Use of gene technology to improve the ability of plants to utilize accumulated forms of soil organic phosphorus
biotechnology
-
the complete hydrolysis of phytate by the enzyme, which is proposed on the basis of its capability to cleave any phosphate group of phytate, is a highly desired property for the biotechnological application of the enzyme
biotechnology
-
potential of using yeast as a phytase carrier in the gastrointestinal tract. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
biotechnology
-
production of phytase in laboratory-scale fermenter. Maintaining an acidic environment (pH 1.5-1.8) in the fermentation broth after the initial buildup of cell mass along with proper fragmentation of filamentous fungi results in significant improvement in phytase productivity
biotechnology
-
high levels of stable phytase is expressed in the culture medium of transgenic Medicago truncatula cell suspension cultures
biotechnology
in vitro digestibility tests show recombinantly expressed phytase is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed and is therefore suitable sources of phytase supplement
biotechnology
in vitro digestibility tests show recombinantly expressed phytase is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed and is therefore suitable sources of phytase supplement
biotechnology
-
phytase from Bacillus subtilis (168phyA) is constitutively expressed in tobacco and Arabidopsis to generate transgenic plants capable of utilizing exogenous phytate. In tobacco, phytase activities in transgenic leaf and root extracts are seven to eight times higher than those in wild-type extracts; whereas, the extracellular phytase activities of transgenic plants are enhanced by four to six times. Similar results are observed from the transgenic Arabidopsis. These results may offer a new perspective on mobilizing soil phytate into inorganic phosphate for plant uptake
biotechnology
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phytase from Bacillus subtilis is introduced into the cytoplasm of tobacco cells that results in equilibrium shift of inositol biosynthesis pathway, thereby making more phosphate available for primary metabolism. The transgenic line exhibit phenotypic changes like increased flowering, lower seed IP6/IP5 ratio, and enhanced growth under phosphate starvation conditions compared to wild type
biotechnology
-
phytase is very suitable to be used in animal feed particularly in common carp feed because of its optimum pH with excellent thermal stability. Bacillus phytase supplementation of 300 U/kg can gain the same result as that of 1000 U/kg supplementation of acidic phytase and neutral phytase supplementation of 1000 U/kg can replace the inorganic phosphorus supplement. A combination of Bacillus phytases and other acidic phytases might induce a more effective hydrolysis of phytate in both the stomach and small intestine of animals in terms of the pH of the animal gastrointestinal tract
biotechnology
-
ten bean cultivars are evaluated for variability in phytate, phenolic, and mineral contents, phytase activity, and antioxidant properties to elucidate the relationship of these components. Multivariate data analysis performed on 22 components analyzed in this study using principal component analysis and cluster methods demonstrate that differences in phytase, antioxidant activity, mineral contents, and bioavailability are much larger within market class than among bean cultivars
biotechnology
Yersinia rohdei phytase is an attractive additive to animal feed
biotechnology
-
in vitro digestibility tests show recombinantly expressed phytase is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed and is therefore suitable sources of phytase supplement
-
biotechnology
-
potential of using yeast as a phytase carrier in the gastrointestinal tract. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
biotechnology
-
phytase is very suitable to be used in animal feed particularly in common carp feed because of its optimum pH with excellent thermal stability. Bacillus phytase supplementation of 300 U/kg can gain the same result as that of 1000 U/kg supplementation of acidic phytase and neutral phytase supplementation of 1000 U/kg can replace the inorganic phosphorus supplement. A combination of Bacillus phytases and other acidic phytases might induce a more effective hydrolysis of phytate in both the stomach and small intestine of animals in terms of the pH of the animal gastrointestinal tract
-
biotechnology
-
ten bean cultivars are evaluated for variability in phytate, phenolic, and mineral contents, phytase activity, and antioxidant properties to elucidate the relationship of these components. Multivariate data analysis performed on 22 components analyzed in this study using principal component analysis and cluster methods demonstrate that differences in phytase, antioxidant activity, mineral contents, and bioavailability are much larger within market class than among bean cultivars
-
biotechnology
-
in vitro digestibility tests show recombinantly expressed phytase is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed and is therefore suitable sources of phytase supplement
-
food industry
-
Pediococcus pentosaceus strains KTU05-9 and KTU05-8 are recommended to use as a starter for sourdough preparation for increasing of mineral bioavailability from wholemeal wheat bread
food industry
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
food industry
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
food industry
-
the enzyme can be applied in dephytinizing animal feeds, and the baking industry. Effect of phytase supplementation in different doses on bread characteristics, overview
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
nutrition
-
moderate decrease of pH by sourdough fermentation is sufficient to reduce phytate content of whole wheat flour through endogenous phytase activity
nutrition
-
due to its specific enzymatic activity, phytase is considered a green feed additive, which can effectively improve the availability of phytate-P and, simultaneously, eliminate the anti-nutritional function of phytate, resulting in a lower production cost and improved environmental protection
nutrition
-
due to its specific enzymatic activity, phytase is considered a green feed additive, which can effectively improve the availability of phytate-P and, simultaneously, eliminate the anti-nutritional function of phytate, resulting in a lower production cost and improved environmental protection
-
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
Schwanniomyces castellii
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
Penicillium caseoicolum
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
Aspergillus syndowi
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
-
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
-